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Comment
. 2016 Oct 4;35(19):2066-2067.
doi: 10.15252/embj.201695385. Epub 2016 Aug 30.

Methionine on the rise: how mitochondria changed their codon usage

Felix Boos  1 , Michael Wollin  1 , Johannes M Herrmann  1
Affiliations
Comment

Methionine on the rise: how mitochondria changed their codon usage

Felix Boos et al. EMBO J. .

Abstract

The tRNA specific for methionine (tRNAM et) of human mitochondria contains a formyl‐cytosine at the wobble position of the anticodon to facilitate its binding to AUG, AUA and (in one instance) to AUU. In this issue of The EMBO Journal, Haag et al identify a two‐step enzyme pathway facilitating the modification of the tRNA. Sequential reactions of the methyltransferase NSUN3 and the dioxygenase ALKBH1/ABH1 are important to render the tRNA as able to recognize the non‐canonical methionine codons AUA and AUUs, a property critical for efficient protein synthesis in human mitochondria.

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Figures

Figure 1
Figure 1. The anticodon of the mitochondrial tRNAMet is modified by two sequential enzymatic reactions
In a first step the cytosine at position 34 in the wobble position of the anticodon is methylated by NSUN3 in a reaction using S‐adenosylmethionine (SAM). Subsequently, the oxygenase ALKBH1/ABH1 converts the methyl‐cytosine to formyl‐cytosine, thereby increasing the spectrum of recognized codons to AUG, AUA and AUU.
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